ArticleNucleic acids research2014
Systematic mutational analysis of the LytTR DNA binding domain of Staphylococcus aureus virulence gene transcription factor AgrA.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Hijacking the signal: a critical evaluation of quorum sensing inhibitors as a next-generation approach against Staphylococcus aureus.Cell communication and signaling : CCS · 2026Review
- A novel insight into ComE-mediated activation of gene expression inMicrobiology spectrum · 2025Article
- Characterization of a MHYT domain-coupled transcriptional regulator that responds to carbon monoxide.Nucleic acids research · 2024Article
- Computational Mutagenesis and Inhibition ofBioMed research international · 2024Article
- Anti-Quorum Sensing Activities of Gliptins againstBiomedicines · 2022Article
- Labdane Diterpenoids fromMolecules (Basel, Switzerland) · 2021Article
- Structural and functional characterization of the bacterial biofilm activator RemA.Nature communications · 2021Article
- A Novel Aza-Derivative InhibitsFrontiers in microbiology · 2021Article
- Discovery of a bacterial peptide as a modulator of GLP-1 and metabolic disease.Scientific reports · 2020Article
- Naturally occurring polymorphisms in the virulence regulator Rsp modulate Staphylococcus aureus survival in blood and antibiotic susceptibility.Microbiology (Reading, England) · 2018Article
- Identification of Staphylococcus aureus Cellular Pathways Affected by the Stilbenoid Lead Drug SK-03-92 Using a Microarray.Antibiotics (Basel, Switzerland) · 2017Article
- Conformational features of theBiochemistry and biophysics reports · 2016Article
- Norlichexanthone Reduces Virulence Gene Expression and Biofilm Formation in Staphylococcus aureus.PloS one · 2016Article
- Insights into the DNA-binding mechanism of a LytTR-type transcription regulator.Bioscience reports · 2016Article
- ω-Hydroxyemodin limits staphylococcus aureus quorum sensing-mediated pathogenesis and inflammation.Antimicrobial agents and chemotherapy · 2015Article
- A novel CO-responsive transcriptional regulator and enhanced H2 production by an engineered Thermococcus onnurineus NA1 strain.Applied and environmental microbiology · 2015Article
- Targeting Virulence inmSphereReview
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Most DNA-binding bacterial transcription factors contact DNA through a recognition α-helix in their DNA-binding domains. An emerging class of DNA-binding transcription factors, predominantly found in pathogenic bacteria interact with the DNA via a relatively novel type of DNA-binding domain, called the LytTR domain, which mainly comprises β strands. Even though the crystal structure of the LytTR domain of the virulence gene transcription factor AgrA from Staphylococcus aureus bound to its cognate DNA sequence is available, the contribution of specific amino acid residues in the LytTR domain of AgrA to transcription activation remains elusive. Here, for the first time, we have systematically investigated the role of amino acid residues in transcription activation in a LytTR domain-containing transcription factor. Our analysis, which involves in vivo and in vitro analyses and molecular dynamics simulations of S. aureus AgrA identifies a highly conserved tyrosine residue, Y229, as a major amino acid determinant for maximal activation of transcription by AgrA and provides novel insights into structure-function relationships in S. aureus AgrA.
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